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Titolo:
EFFICIENT INTERACTION OF THE VESICULAR STOMATITIS-VIRUS P-PROTEIN WITH THE L-PROTEIN OR THE N-PROTEIN IN CELLS EXPRESSING THE RECOMBINANT PROTEINS
Autore:
TAKACS AM; BANERJEE AK;
Indirizzi:
CLEVELAND CLIN FDN,RES INST,DEPT MOLEC BIOL,9500 EUCLID AVE,NC20 CLEVELAND OH 44195 CLEVELAND CLIN FDN,RES INST,DEPT MOLEC BIOL CLEVELAND OH 44195
Titolo Testata:
Virology
fascicolo: 2, volume: 208, anno: 1995,
pagine: 821 - 826
SICI:
0042-6822(1995)208:2<821:EIOTVS>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
EUKARYOTIC TRANSCRIPTIONAL ACTIVATORS; NUCLEOCAPSID PROTEIN; PHOSPHOPROTEIN-P; ACIDIC DOMAIN; MULTIPLE COMPLEXES; GENE-EXPRESSION; RNA-POLYMERASE; GENOME RNA; INVITRO; REPLICATION;
Tipo documento:
Note
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
34
Recensione:
Indirizzi per estratti:
Citazione:
A.M. Takacs e A.K. Banerjee, "EFFICIENT INTERACTION OF THE VESICULAR STOMATITIS-VIRUS P-PROTEIN WITH THE L-PROTEIN OR THE N-PROTEIN IN CELLS EXPRESSING THE RECOMBINANT PROTEINS", Virology, 208(2), 1995, pp. 821-826

Abstract

Specific in vivo interaction between the phosphoprotein (P) and the large polymerase protein (L) from the Indiana serotype of vesicular stomatitis virus was studied using a two-hybrid system. Transfection of CHO cells with plasmids encoding GALP(IND) and VPL(IND) fusion proteinsresulted in an easily detectable level of CAT activity, indicating that P-IND and L(IND) associate in vivo in the absence of other viral proteins. Mutational studies of P-IND demonstrated that both domains I and II of P-IND are important for P-IND-L(IND) association. In addition, casein kinase II (CKII)-mediated phosphorylation within domain I of P-IND was necessary for efficient association with L(IND). We have also used the two-hybrid system to show P-IND interaction with N-IND in vivo. P-IND and N-IND associated more strongly than P-IND and L(IND) A similiar strong association was observed in heterologous interaction studies between Indiana and New Jersey serotype P and N proteins. Mutational studies of FIND demonstrated that, unlike what was found for P-NJ-N-NJ association, only the C-terminal region of the P protein was important for efficient association with N-IND. Like P-NJ, CKII-mediatedphosphorylation within domain I of P-IND was not required for P-N association and, like N-NJ, the C-terminal five amino acids of the N-IND protein were critical for P association with N. These results demonstrate the importance of phosphorylation and specific domains of the P protein in its interaction with the L and N proteins, which are necessary for viral transcription and replication, respectively. (C) 1985 Academic Press, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 22:00:56